Frontiers in the enzymology of thiamin diphosphate-dependent enzymes
S Prajapati, FR von Pappenheim, K Tittmann - Current Opinion in Structural …, 2022 - Elsevier
Enzymes that use thiamin diphosphate (ThDP), the biologically active derivative of vitamin
B1, as a cofactor play important roles in cellular metabolism in all domains of life. The …
B1, as a cofactor play important roles in cellular metabolism in all domains of life. The …
QM/MM study of a VIM-1 metallo-β-lactamase enzyme: The catalytic reaction mechanism
The hydrolysis of carbapenem antibiotics by metallo-β-lactamase enzymes (MBLs) is a
biologically crucial reaction that promotes the antibiotic resistance, and consequently, MBLs …
biologically crucial reaction that promotes the antibiotic resistance, and consequently, MBLs …
Dynamic Protonation States Underlie Carbene Formation in ThDP-Dependent Enzymes: A Theoretical Study
J Uranga, F Rabe von Pappenheim… - The Journal of …, 2023 - ACS Publications
The activation mechanism of thiamine diphosphate (ThDP) in enzymes has long been the
subject of intense research and controversial discussion. Particularly contentious is the …
subject of intense research and controversial discussion. Particularly contentious is the …
QM/MM study of human transketolase: thiamine diphosphate activation mechanism and complete catalytic cycle
L Nauton, L Hecquet, V Théry - Journal of Chemical Information …, 2021 - ACS Publications
A computational model for human transketolase was proposed, showing that thiamine
diphosphate activation was based on His110 in place of His481 reported in yeast …
diphosphate activation was based on His110 in place of His481 reported in yeast …
On the Mechanism of the Lysosomal Enzyme Iduronate‐2‐sulfatase. A Multiscale Approach
Abstract Iduronate‐2‐sulfatase (IDS) is a Ca2+‐dependent enzyme belonging to the family
of sulfatases that catalyzes the hydrolysis of sulphurylated glycosaminoglycans (GAGs), like …
of sulfatases that catalyzes the hydrolysis of sulphurylated glycosaminoglycans (GAGs), like …